HEADER TRANSFERASE 28-FEB-07 2P0E
TITLE HUMAN NICOTINAMIDE RIBOSIDE KINASE 1 IN COMPLEX WITH TIAZOFURIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NICOTINAMIDE RIBOSIDE KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NRK1, C9ORF95;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC
KEYWDS NON-PROTEIN KINASE, NAD+, NICOTINAMIDE RIBOSIDE, NRK1, TIAZOFURIN,
KEYWDS 2 ADP, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.M.RABEH,W.TEMPEL,L.NEDYALKOVA,R.LANDRY,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 2 M.SUNDSTROM,J.WEIGELT,A.BOCHKAREV,C.BRENNER,H.PARK,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 5 03-APR-24 2P0E 1 REMARK SEQADV LINK
REVDAT 4 18-OCT-17 2P0E 1 REMARK
REVDAT 3 24-FEB-09 2P0E 1 VERSN
REVDAT 2 16-OCT-07 2P0E 1 JRNL
REVDAT 1 08-MAY-07 2P0E 0
JRNL AUTH W.TEMPEL,W.M.RABEH,K.L.BOGAN,P.BELENKY,M.WOJCIK,H.F.SEIDLE,
JRNL AUTH 2 L.NEDYALKOVA,T.YANG,A.A.SAUVE,H.W.PARK,C.BRENNER
JRNL TITL NICOTINAMIDE RIBOSIDE KINASE STRUCTURES REVEAL NEW PATHWAYS
JRNL TITL 2 TO NAD(+).
JRNL REF PLOS BIOL. V. 5 E263 2007
JRNL REFN ISSN 1544-9173
JRNL PMID 17914902
JRNL DOI 10.1371/JOURNAL.PBIO.0050263
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 22855
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.167
REMARK 3 FREE R VALUE TEST SET COUNT : 1181
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1561
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1546
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28900
REMARK 3 B22 (A**2) : 0.12400
REMARK 3 B33 (A**2) : -0.41300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.185
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1648 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1115 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2249 ; 1.450 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2719 ; 0.934 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 202 ; 5.477 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 80 ;31.513 ;24.750
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 286 ;12.111 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;16.152 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 246 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1815 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 330 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 288 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1111 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 770 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 767 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 117 ; 0.138 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.071 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 10 ; 0.214 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 38 ; 0.159 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.164 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1085 ; 2.441 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 385 ; 0.685 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1593 ; 3.109 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 763 ; 2.526 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 649 ; 3.571 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. MOLPROBITY, PRODRG, COOT PROGRAMS HAVE ALSO BEEN USED
REMARK 3 IN THE REFINEMENT
REMARK 4
REMARK 4 2P0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041809.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43446
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: SAME PROTEIN IN COMPLEX WITH NICOTINAMIDE
REMARK 200 MONONUCLEOTIDE BASED ON AN ISOMORPHOUS CRYSTAL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M SODIUM PHOSPHATE
REMARK 280 MONOBASIC, 0.1M BICINE, PH 9.0, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.00250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.00250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 27.80400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 70.78550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.80400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 70.78550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.00250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.80400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.78550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 31.00250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.80400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 70.78550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). AUTHORS STATE THAT THE
REMARK 300 BIOLOGICAL UNIT OF THIS PROTEIN IS UNKNOWN.
REMARK 300 THE BIOLOGICAL UNIT ASSEMBLY SHOWN IN REMARK 350 IS
REMARK 300 PREDICTED BY THE ANALYSIS OF PROTEIN INTERFACES BASED ON
REMARK 300 THIS CRYSTAL STRUCTURE.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MSE A -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 LEU A -5
REMARK 465 GLU A 86
REMARK 465 SER A 87
REMARK 465 ALA A 88
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 1 CE NZ
REMARK 470 LYS A 24 CE NZ
REMARK 470 LYS A 48 CD CE NZ
REMARK 470 GLN A 134 CG CD OE1 NE2
REMARK 470 LYS A 152 CD CE NZ
REMARK 470 GLN A 158 CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 UNK UNX A 252 O HOH A 464 1.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 55 45.32 -99.93
REMARK 500 THR A 83 -141.14 -156.10
REMARK 500 HIS A 145 -56.00 -138.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TIZ A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 252
DBREF 2P0E A 1 188 UNP Q9NWW6 NRK1_HUMAN 2 189
SEQADV 2P0E MSE A -18 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E GLY A -17 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E SER A -16 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E SER A -15 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E HIS A -14 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E HIS A -13 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E HIS A -12 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E HIS A -11 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E HIS A -10 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E HIS A -9 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E SER A -8 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E SER A -7 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E GLY A -6 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E LEU A -5 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E VAL A -4 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E PRO A -3 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E ARG A -2 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E GLY A -1 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E SER A 0 UNP Q9NWW6 EXPRESSION TAG
SEQADV 2P0E MSE A 62 UNP Q9NWW6 MET 63 MODIFIED RESIDUE
SEQADV 2P0E MSE A 65 UNP Q9NWW6 MET 66 MODIFIED RESIDUE
SEQADV 2P0E MSE A 66 UNP Q9NWW6 MET 67 MODIFIED RESIDUE
SEQADV 2P0E MSE A 73 UNP Q9NWW6 MET 74 MODIFIED RESIDUE
SEQADV 2P0E MSE A 149 UNP Q9NWW6 MET 150 MODIFIED RESIDUE
SEQADV 2P0E MSE A 157 UNP Q9NWW6 MET 158 MODIFIED RESIDUE
SEQRES 1 A 207 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 207 LEU VAL PRO ARG GLY SER LYS THR PHE ILE ILE GLY ILE
SEQRES 3 A 207 SER GLY VAL THR ASN SER GLY LYS THR THR LEU ALA LYS
SEQRES 4 A 207 ASN LEU GLN LYS HIS LEU PRO ASN CYS SER VAL ILE SER
SEQRES 5 A 207 GLN ASP ASP PHE PHE LYS PRO GLU SER GLU ILE GLU THR
SEQRES 6 A 207 ASP LYS ASN GLY PHE LEU GLN TYR ASP VAL LEU GLU ALA
SEQRES 7 A 207 LEU ASN MSE GLU LYS MSE MSE SER ALA ILE SER CYS TRP
SEQRES 8 A 207 MSE GLU SER ALA ARG HIS SER VAL VAL SER THR ASP GLN
SEQRES 9 A 207 GLU SER ALA GLU GLU ILE PRO ILE LEU ILE ILE GLU GLY
SEQRES 10 A 207 PHE LEU LEU PHE ASN TYR LYS PRO LEU ASP THR ILE TRP
SEQRES 11 A 207 ASN ARG SER TYR PHE LEU THR ILE PRO TYR GLU GLU CYS
SEQRES 12 A 207 LYS ARG ARG ARG SER THR ARG VAL TYR GLN PRO PRO ASP
SEQRES 13 A 207 SER PRO GLY TYR PHE ASP GLY HIS VAL TRP PRO MSE TYR
SEQRES 14 A 207 LEU LYS TYR ARG GLN GLU MSE GLN ASP ILE THR TRP GLU
SEQRES 15 A 207 VAL VAL TYR LEU ASP GLY THR LYS SER GLU GLU ASP LEU
SEQRES 16 A 207 PHE LEU GLN VAL TYR GLU ASP LEU ILE GLN GLU LEU
MODRES 2P0E MSE A 62 MET SELENOMETHIONINE
MODRES 2P0E MSE A 65 MET SELENOMETHIONINE
MODRES 2P0E MSE A 66 MET SELENOMETHIONINE
MODRES 2P0E MSE A 73 MET SELENOMETHIONINE
MODRES 2P0E MSE A 149 MET SELENOMETHIONINE
MODRES 2P0E MSE A 157 MET SELENOMETHIONINE
HET MSE A 62 8
HET MSE A 65 8
HET MSE A 66 8
HET MSE A 73 8
HET MSE A 149 8
HET MSE A 157 8
HET PO4 A 202 5
HET CL A 251 1
HET TIZ A 201 17
HET UNX A 252 1
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETNAM TIZ (1R)-1-[4-(AMINOCARBONYL)-1,3-THIAZOL-2-YL]-1,4-
HETNAM 2 TIZ ANHYDRO-D-RIBITOL
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN TIZ TIAZOFURIN
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 PO4 O4 P 3-
FORMUL 3 CL CL 1-
FORMUL 4 TIZ C9 H12 N2 O5 S
FORMUL 5 UNX X
FORMUL 6 HOH *166(H2 O)
HELIX 1 1 GLY A 14 LYS A 24 1 11
HELIX 2 2 ASP A 35 PHE A 38 5 4
HELIX 3 3 PRO A 40 ILE A 44 5 5
HELIX 4 4 VAL A 56 LEU A 60 5 5
HELIX 5 5 ASN A 61 ARG A 77 1 17
HELIX 6 6 TYR A 104 ASP A 108 5 5
HELIX 7 7 PRO A 120 ARG A 131 1 12
HELIX 8 8 GLY A 140 HIS A 145 1 6
HELIX 9 9 HIS A 145 GLN A 158 1 14
HELIX 10 10 SER A 172 GLN A 186 1 15
SHEET 1 A 5 CYS A 29 SER A 33 0
SHEET 2 A 5 ILE A 93 GLU A 97 1 O ILE A 95 N SER A 30
SHEET 3 A 5 PHE A 3 GLY A 9 1 N ILE A 5 O ILE A 96
SHEET 4 A 5 ARG A 113 THR A 118 1 O TYR A 115 N SER A 8
SHEET 5 A 5 VAL A 165 ASP A 168 1 O LEU A 167 N PHE A 116
LINK C ASN A 61 N MSE A 62 1555 1555 1.32
LINK C MSE A 62 N GLU A 63 1555 1555 1.33
LINK C LYS A 64 N MSE A 65 1555 1555 1.34
LINK C MSE A 65 N MSE A 66 1555 1555 1.33
LINK C MSE A 66 N SER A 67 1555 1555 1.33
LINK C TRP A 72 N MSE A 73 1555 1555 1.32
LINK C MSE A 73 N GLU A 74 1555 1555 1.33
LINK C PRO A 148 N MSE A 149 1555 1555 1.32
LINK C MSE A 149 N TYR A 150 1555 1555 1.33
LINK C GLU A 156 N MSE A 157 1555 1555 1.34
LINK C MSE A 157 N GLN A 158 1555 1555 1.33
CISPEP 1 GLN A 134 PRO A 135 0 4.13
SITE 1 AC1 9 ASN A 12 SER A 13 GLY A 14 LYS A 15
SITE 2 AC1 9 THR A 16 ARG A 131 HOH A 302 HOH A 382
SITE 3 AC1 9 HOH A 424
SITE 1 AC2 3 SER A 82 HOH A 335 HOH A 352
SITE 1 AC3 9 ASP A 35 PHE A 38 TYR A 54 ASP A 55
SITE 2 AC3 9 PHE A 99 ARG A 128 GLN A 134 HOH A 382
SITE 3 AC3 9 HOH A 385
SITE 1 AC4 5 HOH A 383 HOH A 449 HOH A 450 HOH A 463
SITE 2 AC4 5 HOH A 464
CRYST1 55.608 141.571 62.005 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017980 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007060 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016130 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
